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The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels
Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels control spontaneous electrical activity in heart and brain. Binding of cAMP to the cyclic nucleotide-binding domain (CNBD) facilitates channel opening by relieving a tonic inhibition exerted by the CNBD. Despite high resolution struc...
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| Published in: | eLife 2019-11, Vol.8 |
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| creator | Porro, Alessandro Saponaro, Andrea Gasparri, Federica Bauer, Daniel Gross, Christine Pisoni, Matteo Abbandonato, Gerardo Hamacher, Kay Santoro, Bina Thiel, Gerhard Moroni, Anna |
| description | Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels control spontaneous electrical activity in heart and brain. Binding of cAMP to the cyclic nucleotide-binding domain (CNBD) facilitates channel opening by relieving a tonic inhibition exerted by the CNBD. Despite high resolution structures of the HCN1 channel in the cAMP bound and unbound states, the structural mechanism coupling ligand binding to channel gating is unknown. Here we show that the recently identified helical HCN-domain (HCND) mechanically couples the CNBD and channel voltage sensing domain (VSD), possibly acting as a sliding crank that converts the planar rotational movement of the CNBD into a rotational upward displacement of the VSD. This mode of operation and its impact on channel gating are confirmed by computational and experimental data showing that disruption of critical contacts between the three domains affects cAMP- and voltage-dependent gating in three HCN isoforms. |
| doi_str_mv | 10.7554/eLife.49672 |
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Binding of cAMP to the cyclic nucleotide-binding domain (CNBD) facilitates channel opening by relieving a tonic inhibition exerted by the CNBD. Despite high resolution structures of the HCN1 channel in the cAMP bound and unbound states, the structural mechanism coupling ligand binding to channel gating is unknown. Here we show that the recently identified helical HCN-domain (HCND) mechanically couples the CNBD and channel voltage sensing domain (VSD), possibly acting as a sliding crank that converts the planar rotational movement of the CNBD into a rotational upward displacement of the VSD. This mode of operation and its impact on channel gating are confirmed by computational and experimental data showing that disruption of critical contacts between the three domains affects cAMP- and voltage-dependent gating in three HCN isoforms.</description><identifier>ISSN: 2050-084X</identifier><identifier>EISSN: 2050-084X</identifier><identifier>DOI: 10.7554/eLife.49672</identifier><identifier>PMID: 31769408</identifier><language>eng</language><publisher>England: eLife Science Publications, Ltd</publisher><subject>Binding Sites ; cAMP ; Cardiology ; Channel gating ; Channel opening ; Computational neuroscience ; Cyclic adenosine monophosphate ; Cyclic AMP ; Cyclic AMP - chemistry ; Cyclic AMP - metabolism ; Electrophysiology ; gating ; HCN ; HCN domain ; HEK293 Cells - physiology ; Humans ; Hydrophobic and Hydrophilic Interactions ; Hyperpolarization ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - chemistry ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - genetics ; Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - metabolism ; Ion Channel Gating ; Ion channels (cyclic nucleotide-gated) ; Isoforms ; Kinetics ; Molecular Dynamics Simulation ; N terminus ; Physiology ; Protein Conformation ; Protein Domains ; Protein Isoforms ; Regulation ; Sensors ; Structural Biology and Molecular Biophysics ; Thermodynamics ; Ventricular septal defects ; Voltage</subject><ispartof>eLife, 2019-11, Vol.8</ispartof><rights>2019, Porro et al.</rights><rights>COPYRIGHT 2019 eLife Science Publications, Ltd.</rights><rights>2019, Porro et al. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2019, Porro et al 2019 Porro et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-e0d357d8e0f6843866115aaa0e69b59588bfe1688cd0bdb5434ecc4cc60eed993</citedby><cites>FETCH-LOGICAL-c576t-e0d357d8e0f6843866115aaa0e69b59588bfe1688cd0bdb5434ecc4cc60eed993</cites><orcidid>0000-0001-5035-5174 ; 0000-0002-4277-1992 ; 0000-0002-1860-406X ; 0000-0003-4845-6165 ; 0000-0001-7247-051X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2331591560/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2331591560?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,25731,27901,27902,36989,36990,44566,53766,53768,74869</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/31769408$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Porro, Alessandro</creatorcontrib><creatorcontrib>Saponaro, Andrea</creatorcontrib><creatorcontrib>Gasparri, Federica</creatorcontrib><creatorcontrib>Bauer, Daniel</creatorcontrib><creatorcontrib>Gross, Christine</creatorcontrib><creatorcontrib>Pisoni, Matteo</creatorcontrib><creatorcontrib>Abbandonato, Gerardo</creatorcontrib><creatorcontrib>Hamacher, Kay</creatorcontrib><creatorcontrib>Santoro, Bina</creatorcontrib><creatorcontrib>Thiel, Gerhard</creatorcontrib><creatorcontrib>Moroni, Anna</creatorcontrib><title>The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels</title><title>eLife</title><addtitle>Elife</addtitle><description>Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels control spontaneous electrical activity in heart and brain. Binding of cAMP to the cyclic nucleotide-binding domain (CNBD) facilitates channel opening by relieving a tonic inhibition exerted by the CNBD. Despite high resolution structures of the HCN1 channel in the cAMP bound and unbound states, the structural mechanism coupling ligand binding to channel gating is unknown. Here we show that the recently identified helical HCN-domain (HCND) mechanically couples the CNBD and channel voltage sensing domain (VSD), possibly acting as a sliding crank that converts the planar rotational movement of the CNBD into a rotational upward displacement of the VSD. This mode of operation and its impact on channel gating are confirmed by computational and experimental data showing that disruption of critical contacts between the three domains affects cAMP- and voltage-dependent gating in three HCN isoforms.</description><subject>Binding Sites</subject><subject>cAMP</subject><subject>Cardiology</subject><subject>Channel gating</subject><subject>Channel opening</subject><subject>Computational neuroscience</subject><subject>Cyclic adenosine monophosphate</subject><subject>Cyclic AMP</subject><subject>Cyclic AMP - chemistry</subject><subject>Cyclic AMP - metabolism</subject><subject>Electrophysiology</subject><subject>gating</subject><subject>HCN</subject><subject>HCN domain</subject><subject>HEK293 Cells - physiology</subject><subject>Humans</subject><subject>Hydrophobic and Hydrophilic Interactions</subject><subject>Hyperpolarization</subject><subject>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - chemistry</subject><subject>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - genetics</subject><subject>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - metabolism</subject><subject>Ion Channel Gating</subject><subject>Ion channels (cyclic nucleotide-gated)</subject><subject>Isoforms</subject><subject>Kinetics</subject><subject>Molecular Dynamics Simulation</subject><subject>N terminus</subject><subject>Physiology</subject><subject>Protein Conformation</subject><subject>Protein Domains</subject><subject>Protein Isoforms</subject><subject>Regulation</subject><subject>Sensors</subject><subject>Structural Biology and Molecular Biophysics</subject><subject>Thermodynamics</subject><subject>Ventricular septal defects</subject><subject>Voltage</subject><issn>2050-084X</issn><issn>2050-084X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><sourceid>DOA</sourceid><recordid>eNptkk2P0zAQhiMEYlfLnrijSFxAKMWuP-JckKoK2ErlQ7BI3CzHnqSuUjtrJ4Xy63HbZdki7INH42dej0dvlj3FaFIyRl_D0jYwoRUvpw-y8yliqECCfn94Lz7LLmNco7RKKgSuHmdnBJe8okicZz-uV5BfzT_mxm-Udbn2Y99BzLe-G1QLeasG69pcOZPr2YfPeYDYexchT-xq10PofaeC_ZUw7wqlB7tVAyR4pzurczfqDvxgDRTtMb9SzkEXn2SPGtVFuLw9L7Jv795ez6-K5af3i_lsWWhW8qEAZAgrjQDUcEGJ4BxjppRCwKuaVUyIugHMhdAG1aZmlFDQmmrNEYCpKnKRLY66xqu17IPdqLCTXll5SPjQShUGm7qUlWgYxjXHQBAVHCkBNRKqNIbVhBGetN4ctfqx3oDR4IaguhPR0xtnV7L1W8lFRatpmQRe3AoEfzNCHOTGRg1dpxz4McopwaKkjAic0Of_oGs_BpdGlSiCWYUZR3-pVqUPWNf49K7ei8oZRyWnYlru-578h0rbwMZq76CxKX9S8PKkIDED_BxaNcYoF1-_nLKvjqwOPsYAzd08MJJ7i8qDReXBool-dn-Ed-wfQ5LffpbhYA</recordid><startdate>20191126</startdate><enddate>20191126</enddate><creator>Porro, Alessandro</creator><creator>Saponaro, Andrea</creator><creator>Gasparri, Federica</creator><creator>Bauer, Daniel</creator><creator>Gross, Christine</creator><creator>Pisoni, Matteo</creator><creator>Abbandonato, Gerardo</creator><creator>Hamacher, Kay</creator><creator>Santoro, Bina</creator><creator>Thiel, Gerhard</creator><creator>Moroni, Anna</creator><general>eLife Science Publications, Ltd</general><general>eLife Sciences Publications Ltd</general><general>eLife Sciences Publications, Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>ISR</scope><scope>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope><orcidid>https://orcid.org/0000-0001-5035-5174</orcidid><orcidid>https://orcid.org/0000-0002-4277-1992</orcidid><orcidid>https://orcid.org/0000-0002-1860-406X</orcidid><orcidid>https://orcid.org/0000-0003-4845-6165</orcidid><orcidid>https://orcid.org/0000-0001-7247-051X</orcidid></search><sort><creationdate>20191126</creationdate><title>The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels</title><author>Porro, Alessandro ; Saponaro, Andrea ; Gasparri, Federica ; Bauer, Daniel ; Gross, Christine ; Pisoni, Matteo ; Abbandonato, Gerardo ; Hamacher, Kay ; Santoro, Bina ; Thiel, Gerhard ; Moroni, Anna</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c576t-e0d357d8e0f6843866115aaa0e69b59588bfe1688cd0bdb5434ecc4cc60eed993</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Binding Sites</topic><topic>cAMP</topic><topic>Cardiology</topic><topic>Channel gating</topic><topic>Channel opening</topic><topic>Computational neuroscience</topic><topic>Cyclic adenosine monophosphate</topic><topic>Cyclic AMP</topic><topic>Cyclic AMP - chemistry</topic><topic>Cyclic AMP - metabolism</topic><topic>Electrophysiology</topic><topic>gating</topic><topic>HCN</topic><topic>HCN domain</topic><topic>HEK293 Cells - physiology</topic><topic>Humans</topic><topic>Hydrophobic and Hydrophilic Interactions</topic><topic>Hyperpolarization</topic><topic>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - chemistry</topic><topic>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - genetics</topic><topic>Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - metabolism</topic><topic>Ion Channel Gating</topic><topic>Ion channels (cyclic nucleotide-gated)</topic><topic>Isoforms</topic><topic>Kinetics</topic><topic>Molecular Dynamics Simulation</topic><topic>N terminus</topic><topic>Physiology</topic><topic>Protein Conformation</topic><topic>Protein Domains</topic><topic>Protein Isoforms</topic><topic>Regulation</topic><topic>Sensors</topic><topic>Structural Biology and Molecular Biophysics</topic><topic>Thermodynamics</topic><topic>Ventricular septal defects</topic><topic>Voltage</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Porro, Alessandro</creatorcontrib><creatorcontrib>Saponaro, Andrea</creatorcontrib><creatorcontrib>Gasparri, Federica</creatorcontrib><creatorcontrib>Bauer, Daniel</creatorcontrib><creatorcontrib>Gross, Christine</creatorcontrib><creatorcontrib>Pisoni, Matteo</creatorcontrib><creatorcontrib>Abbandonato, Gerardo</creatorcontrib><creatorcontrib>Hamacher, Kay</creatorcontrib><creatorcontrib>Santoro, Bina</creatorcontrib><creatorcontrib>Thiel, Gerhard</creatorcontrib><creatorcontrib>Moroni, Anna</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>eLife</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Porro, Alessandro</au><au>Saponaro, Andrea</au><au>Gasparri, Federica</au><au>Bauer, Daniel</au><au>Gross, Christine</au><au>Pisoni, Matteo</au><au>Abbandonato, Gerardo</au><au>Hamacher, Kay</au><au>Santoro, Bina</au><au>Thiel, Gerhard</au><au>Moroni, Anna</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels</atitle><jtitle>eLife</jtitle><addtitle>Elife</addtitle><date>2019-11-26</date><risdate>2019</risdate><volume>8</volume><issn>2050-084X</issn><eissn>2050-084X</eissn><abstract>Hyperpolarization-activated cyclic nucleotide-gated (HCN) channels control spontaneous electrical activity in heart and brain. Binding of cAMP to the cyclic nucleotide-binding domain (CNBD) facilitates channel opening by relieving a tonic inhibition exerted by the CNBD. Despite high resolution structures of the HCN1 channel in the cAMP bound and unbound states, the structural mechanism coupling ligand binding to channel gating is unknown. Here we show that the recently identified helical HCN-domain (HCND) mechanically couples the CNBD and channel voltage sensing domain (VSD), possibly acting as a sliding crank that converts the planar rotational movement of the CNBD into a rotational upward displacement of the VSD. This mode of operation and its impact on channel gating are confirmed by computational and experimental data showing that disruption of critical contacts between the three domains affects cAMP- and voltage-dependent gating in three HCN isoforms.</abstract><cop>England</cop><pub>eLife Science Publications, Ltd</pub><pmid>31769408</pmid><doi>10.7554/eLife.49672</doi><orcidid>https://orcid.org/0000-0001-5035-5174</orcidid><orcidid>https://orcid.org/0000-0002-4277-1992</orcidid><orcidid>https://orcid.org/0000-0002-1860-406X</orcidid><orcidid>https://orcid.org/0000-0003-4845-6165</orcidid><orcidid>https://orcid.org/0000-0001-7247-051X</orcidid><oa>free_for_read</oa></addata></record> |
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| source | Publicly Available Content Database; PubMed Central |
| subjects | Binding Sites cAMP Cardiology Channel gating Channel opening Computational neuroscience Cyclic adenosine monophosphate Cyclic AMP Cyclic AMP - chemistry Cyclic AMP - metabolism Electrophysiology gating HCN HCN domain HEK293 Cells - physiology Humans Hydrophobic and Hydrophilic Interactions Hyperpolarization Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - chemistry Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - genetics Hyperpolarization-Activated Cyclic Nucleotide-Gated Channels - metabolism Ion Channel Gating Ion channels (cyclic nucleotide-gated) Isoforms Kinetics Molecular Dynamics Simulation N terminus Physiology Protein Conformation Protein Domains Protein Isoforms Regulation Sensors Structural Biology and Molecular Biophysics Thermodynamics Ventricular septal defects Voltage |
| title | The HCN domain couples voltage gating and cAMP response in hyperpolarization-activated cyclic nucleotide-gated channels |
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